Nicastrin functions as a gamma-secretase-substrate receptor (Q46646587)

23 December 2017

title

Nicastrin functions as a gamma-secretase-substrate receptor (English)

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23 December 2017

9

Thomas Südhof

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23 December 2017

3

Katsuhiko Tabuchi

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23 December 2017

author name string

Sanjiv Shah

1

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23 December 2017

Sheu-Fen Lee

2

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Yi-Heng Hao

4

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23 December 2017

Cong Yu

5

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Quincey LaPlant

6

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23 December 2017

Haydn Ball

7

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23 December 2017

Charles E Dann

8

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23 December 2017

Gang Yu

10

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23 December 2017

language of work or name

English

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publication date

1 August 2005

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23 December 2017

number of pages

13

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published in

Cell

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23 December 2017

volume

122

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23 December 2017

issue

3

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23 December 2017

page(s)

435-447

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Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and betaAPP processing

cites work

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Requirements for signal peptide peptidase-catalyzed intramembrane proteolysis

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Presenilin complexes with the C-terminal fragments of amyloid precursor protein at the sites of amyloid beta-protein generation

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A conserved GXXXG motif in APH-1 is critical for assembly and activity of the gamma-secretase complex

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Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein

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A glutamate residue contributes to the exopeptidase specificity in aminopeptidase A

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Gamma-secretase: proteasome of the membrane?

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Identification of signal peptide peptidase, a presenilin-type aspartic protease

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Synthesis of native proteins by chemical ligation

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Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity

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The initial substrate-binding site of gamma-secretase is located on presenilin near the active site

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Mutation of active site residues of the puromycin-sensitive aminopeptidase: conversion of the enzyme into a catalytically inactive binding protein.

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Mechanism of the cleavage specificity of Alzheimer's disease gamma-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein

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Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases

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Nicastrin, a presenilin-interacting protein, contains an aminopeptidase/transferrin receptor superfamily domain

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A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60

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Substrate specificity of rhomboid intramembrane proteases is governed by helix-breaking residues in the substrate transmembrane domain

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gamma-Secretase activity requires the presenilin-dependent trafficking of nicastrin through the Golgi apparatus but not its complex glycosylation

1 reference

11 October 2022

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The presenilin 1 protein is a component of a high molecular weight intracellular complex that contains beta-catenin

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Characterization of Glu350 as a critical residue involved in the N-terminal amine binding site of aminopeptidase N (EC 3.4.11.2): insights into its mechanism of action

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Nicastrin binds to membrane-tethered Notch

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Immature nicastrin stabilizes APH-1 independent of PEN-2 and presenilin: identification of nicastrin mutants that selectively interact with APH-1.

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11 October 2022

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Mammalian APH-1 interacts with presenilin and nicastrin and is required for intramembrane proteolysis of amyloid-beta precursor protein and Notch

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.CELL.2005.05.022

Asparagine-proline sequence within membrane-spanning segment of SREBP triggers intramembrane cleavage by site-2 protease

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.CELL.2005.05.022

Drosophila rhomboid-1 defines a family of putative intramembrane serine proteases

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.CELL.2005.05.022

Partial Purification and Characterization of γ-Secretase from Post-mortem Human Brain

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.CELL.2005.05.022

A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.CELL.2005.05.022

Identifiers

DOI

10.1016/J.CELL.2005.05.022

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23 December 2017

PubMed ID

16096062

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23 December 2017